RLA1_DROME
ID RLA1_DROME Reviewed; 112 AA.
AC P08570; Q9VPP6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=60S acidic ribosomal protein P1;
DE AltName: Full=Acidic ribosomal protein RPA2;
DE AltName: Full=RP21C;
GN Name=RpLP1; Synonyms=M(2)21C, rp21C, RPA2, RpP2; ORFNames=CG4087;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3122177; DOI=10.1093/nar/15.23.10064;
RA Wigboldus J.D.;
RT "cDNA and deduced amino acid sequence of Drosophila rp21C, another 'A'-type
RT ribosomal protein.";
RL Nucleic Acids Res. 15:10064-10064(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8501137; DOI=10.1002/jcb.240510315;
RA Olson P.F., Salo T., Garrison K., Fessler J.H.;
RT "Drosophila acidic ribosomal protein rpA2: sequence and characterization.";
RL J. Cell. Biochem. 51:353-359(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Plays an important role in the elongation step of protein
CC synthesis.
CC -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC -!- INTERACTION:
CC P08570; P19889: RpLP0; NbExp=4; IntAct=EBI-125901, EBI-195497;
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC {ECO:0000305}.
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DR EMBL; Y00504; CAA68557.1; -; mRNA.
DR EMBL; S62170; AAB26902.1; -; mRNA.
DR EMBL; AE014134; AAF51499.1; -; Genomic_DNA.
DR EMBL; AY069125; AAL39270.1; -; mRNA.
DR PIR; S00659; R5FF2E.
DR RefSeq; NP_001259822.1; NM_001272893.1.
DR RefSeq; NP_476630.1; NM_057282.4.
DR AlphaFoldDB; P08570; -.
DR SMR; P08570; -.
DR BioGRID; 59470; 140.
DR DIP; DIP-18310N; -.
DR IntAct; P08570; 13.
DR STRING; 7227.FBpp0304265; -.
DR iPTMnet; P08570; -.
DR PaxDb; P08570; -.
DR PRIDE; P08570; -.
DR DNASU; 33214; -.
DR EnsemblMetazoa; FBtr0078056; FBpp0077716; FBgn0002593.
DR EnsemblMetazoa; FBtr0331932; FBpp0304265; FBgn0002593.
DR GeneID; 33214; -.
DR KEGG; dme:Dmel_CG4087; -.
DR CTD; 6176; -.
DR FlyBase; FBgn0002593; RpLP1.
DR VEuPathDB; VectorBase:FBgn0002593; -.
DR eggNOG; KOG1762; Eukaryota.
DR GeneTree; ENSGT00940000170577; -.
DR HOGENOM; CLU_114656_1_2_1; -.
DR InParanoid; P08570; -.
DR OMA; EYIYAAM; -.
DR OrthoDB; 1633925at2759; -.
DR PhylomeDB; P08570; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P08570; -.
DR BioGRID-ORCS; 33214; 1 hit in 1 CRISPR screen.
DR ChiTaRS; RpLP1; fly.
DR GenomeRNAi; 33214; -.
DR PRO; PR:P08570; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002593; Expressed in egg cell and 24 other tissues.
DR ExpressionAtlas; P08570; baseline and differential.
DR Genevisible; P08570; DM.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR Gene3D; 1.10.10.1410; -; 1.
DR HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR InterPro; IPR038716; P1/P2_N_sf.
DR InterPro; IPR027534; Ribosomal_L12/P1/P2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..112
FT /note="60S acidic ribosomal protein P1"
FT /id="PRO_0000157692"
FT REGION 80..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 9
FT /note="C -> S (in Ref. 1; CAA68557)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="G -> A (in Ref. 1; CAA68557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 11513 MW; 2EA9CA3E884A7CCF CRC64;
MSTKAELACV YASLILVDDD VAVTGEKINT ILKAANVEVE PYWPGLFAKA LEGINVKDLI
TNIGSGVGAA PAGGAAPAAA AAAPAAESKK EEKKKEEESD QSDDDMGFGL FD
